Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY
Volume 112, Issue -, Pages 16-22Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2012.04.001
Keywords
Morin; Bovine serum albumin; Conformational investigation; Binding parameters; Structure-affinity relationship
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Funding
- National Natural Science Foundation of China [20803019]
- Natural Science Foundation of Hubei Province, China [2010CDB00101]
- Research Foundation of Education Bureau of Hubei Province, China [Q20122205, B20122202]
- Hubei Normal University Foundation, China [2007F10]
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The interaction between morin and bovine serum albumin (BSA) was studied using molecular spectroscopic approach at different temperatures under imitated physiological conditions. Quenching of intrinsic tryptophanyl fluorescence of BSA with increasing morin concentration is the actuating tool in the analysis. The obtained quenching mechanisms, binding constants, binding sites and corresponding thermodynamic parameters at different temperatures indicate that the hydrophobic interaction play a major role in the morin-BSA association. Binding affinity between morin and BSA was determined using Scatchard equation and the modified Stern-Volmer equation, and the corresponding Structure-affinity relationships of flavonoids were discussed. Site marker competitive displacement experiments demonstrated that morin binds with high affinity to site II (subdomain IIIA) of BSA. Furthermore, the circular dichroism spectral results indicated that the conformation of BSA changed in the presence of morin. In addition, the effect of some common metal ions on the binding constant between morin and BSA was examined. (c) 2012 Elsevier B.V. All rights reserved.
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